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P19784

- CSK22_HUMAN

UniProt

P19784 - CSK22_HUMAN

Protein

Casein kinase II subunit alpha'

Gene

CSNK2A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 691ATPPROSITE-ProRule annotation
    Active sitei157 – 1571Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi46 – 549ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein N-terminus binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. axon guidance Source: Reactome
    3. mitotic cell cycle Source: Reactome
    4. mitotic spindle checkpoint Source: UniProtKB
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. transcription, DNA-templated Source: UniProtKB-KW
    7. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.
    REACT_200668. WNT mediated activation of DVL.
    REACT_22272. Signal transduction by L1.
    SignaLinkiP19784.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Casein kinase II subunit alpha' (EC:2.7.11.1)
    Short name:
    CK II alpha'
    Gene namesi
    Name:CSNK2A2
    Synonyms:CK2A2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:2459. CSNK2A2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26959.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 350350Casein kinase II subunit alpha'PRO_0000085891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphotyrosine1 Publication
    Modified residuei18 – 181Phosphoserine2 Publications
    Modified residuei21 – 211Phosphoserine2 Publications
    Modified residuei97 – 971N6-acetyllysine1 Publication
    Modified residuei288 – 2881Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP19784.
    PaxDbiP19784.
    PeptideAtlasiP19784.
    PRIDEiP19784.

    2D gel databases

    SWISS-2DPAGEP19784.

    PTM databases

    PhosphoSiteiP19784.

    Expressioni

    Gene expression databases

    ArrayExpressiP19784.
    BgeeiP19784.
    CleanExiHS_CSNK2A2.
    GenevestigatoriP19784.

    Interactioni

    Subunit structurei

    Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSNK2A1P684003EBI-347451,EBI-347804
    CSNK2BP678706EBI-347451,EBI-348169
    KIF5CO602824EBI-347451,EBI-717170

    Protein-protein interaction databases

    BioGridi107842. 125 interactions.
    DIPiDIP-318N.
    IntActiP19784. 93 interactions.
    MINTiMINT-5004107.
    STRINGi9606.ENSP00000262506.

    Structurei

    Secondary structure

    1
    350
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 133
    Turni14 – 163
    Helixi17 – 193
    Helixi22 – 254
    Helixi27 – 293
    Helixi37 – 393
    Beta strandi40 – 489
    Beta strandi50 – 5910
    Turni60 – 634
    Beta strandi64 – 718
    Helixi76 – 8813
    Turni89 – 913
    Beta strandi98 – 1036
    Turni105 – 1073
    Beta strandi110 – 1156
    Helixi122 – 1254
    Helixi131 – 15020
    Helixi160 – 1623
    Beta strandi163 – 1664
    Turni167 – 1704
    Beta strandi171 – 1744
    Helixi196 – 1983
    Helixi201 – 2044
    Helixi213 – 22816
    Beta strandi231 – 2344
    Helixi239 – 25012
    Helixi252 – 26110
    Helixi270 – 2734
    Helixi282 – 2854
    Turni288 – 2903
    Helixi291 – 2933
    Helixi296 – 30510
    Turni310 – 3123
    Helixi316 – 3205
    Helixi323 – 3253
    Helixi326 – 3316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E3BX-ray3.20X1-334[»]
    3OFMX-ray2.00A1-350[»]
    3U87X-ray2.90A/B327-350[»]
    ProteinModelPortaliP19784.
    SMRiP19784. Positions 8-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19784.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 325286Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233021.
    HOVERGENiHBG107282.
    InParanoidiP19784.
    KOiK03097.
    OMAiPSWGNQD.
    OrthoDBiEOG7QG446.
    PhylomeDBiP19784.
    TreeFamiTF300483.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19784-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK    50
    YSEVFEAINI TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID 100
    TVKDPVSKTP ALVFEYINNT DFKQLYQILT DFDIRFYMYE LLKALDYCHS 150
    KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA EFYHPAQEYN VRVASRYFKG 200
    PELLVDYQMY DYSLDMWSLG CMLASMIFRR EPFFHGQDNY DQLVRIAKVL 250
    GTEELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD 300
    LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCADNA VLSSGLTAAR 350
    Length:350
    Mass (Da):41,213
    Last modified:February 1, 1991 - v1
    Checksum:i3ECB92F6BD3DD7F1
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti188 – 1881E → A.1 Publication
    Corresponds to variant rs55911801 [ dbSNP | Ensembl ].
    VAR_040416

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55268 mRNA. Translation: AAA51548.1.
    BC008812 mRNA. Translation: AAH08812.1.
    CCDSiCCDS10794.1.
    PIRiB35838.
    RefSeqiNP_001887.1. NM_001896.2.
    UniGeneiHs.82201.

    Genome annotation databases

    EnsembliENST00000262506; ENSP00000262506; ENSG00000070770.
    GeneIDi1459.
    KEGGihsa:1459.
    UCSCiuc002enc.3. human.

    Polymorphism databases

    DMDMi125266.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55268 mRNA. Translation: AAA51548.1 .
    BC008812 mRNA. Translation: AAH08812.1 .
    CCDSi CCDS10794.1.
    PIRi B35838.
    RefSeqi NP_001887.1. NM_001896.2.
    UniGenei Hs.82201.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3E3B X-ray 3.20 X 1-334 [» ]
    3OFM X-ray 2.00 A 1-350 [» ]
    3U87 X-ray 2.90 A/B 327-350 [» ]
    ProteinModelPortali P19784.
    SMRi P19784. Positions 8-332.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107842. 125 interactions.
    DIPi DIP-318N.
    IntActi P19784. 93 interactions.
    MINTi MINT-5004107.
    STRINGi 9606.ENSP00000262506.

    Chemistry

    BindingDBi P19784.
    ChEMBLi CHEMBL4070.
    GuidetoPHARMACOLOGYi 1550.

    PTM databases

    PhosphoSitei P19784.

    Polymorphism databases

    DMDMi 125266.

    2D gel databases

    SWISS-2DPAGE P19784.

    Proteomic databases

    MaxQBi P19784.
    PaxDbi P19784.
    PeptideAtlasi P19784.
    PRIDEi P19784.

    Protocols and materials databases

    DNASUi 1459.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262506 ; ENSP00000262506 ; ENSG00000070770 .
    GeneIDi 1459.
    KEGGi hsa:1459.
    UCSCi uc002enc.3. human.

    Organism-specific databases

    CTDi 1459.
    GeneCardsi GC16M058191.
    HGNCi HGNC:2459. CSNK2A2.
    MIMi 115442. gene.
    neXtProti NX_P19784.
    PharmGKBi PA26959.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233021.
    HOVERGENi HBG107282.
    InParanoidi P19784.
    KOi K03097.
    OMAi PSWGNQD.
    OrthoDBi EOG7QG446.
    PhylomeDBi P19784.
    TreeFami TF300483.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.
    REACT_200668. WNT mediated activation of DVL.
    REACT_22272. Signal transduction by L1.
    SignaLinki P19784.

    Miscellaneous databases

    ChiTaRSi CSNK2A2. human.
    EvolutionaryTracei P19784.
    GeneWikii CSNK2A2.
    GenomeRNAii 1459.
    NextBioi 5997.
    PROi P19784.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19784.
    Bgeei P19784.
    CleanExi HS_CSNK2A2.
    Genevestigatori P19784.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II."
      Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A., Krebs E.G.
      Biochemistry 29:8436-8447(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Ovary.
    3. "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1."
      Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H.
      Mol. Cell 7:283-292(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
    4. "Protein kinase CK2 is involved in G2 arrest and apoptosis following spindle damage in epithelial cells."
      Sayed M., Pelech S., Wong C., Marotta A., Salh B.
      Oncogene 20:6994-7005(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL CYCLE.
    5. "p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex."
      Keller D.M., Lu H.
      J. Biol. Chem. 277:50206-50213(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
    6. "Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8."
      Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.
      EMBO J. 24:3532-3542(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS.
    7. "One-thousand-and-one substrates of protein kinase CK2?"
      Meggio F., Pinna L.A.
      FASEB J. 17:349-368(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21 AND SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Protein kinase CK2 in health and disease: Protein kinase CK2: from structures to insights."
      Niefind K., Raaf J., Issinger O.G.
      Cell. Mol. Life Sci. 66:1800-1816(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON STRUCTURE.
    10. "Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival."
      St-Denis N.A., Litchfield D.W.
      Cell. Mol. Life Sci. 66:1817-1829(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    11. "Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: a dynamic affair."
      Filhol O., Cochet C.
      Cell. Mol. Life Sci. 66:1830-1839(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    12. "Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery."
      Miyata Y.
      Cell. Mol. Life Sci. 66:1840-1849(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN REGULATION OF HSP90.
    13. "Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: linking development and cancer."
      Dominguez I., Sonenshein G.E., Seldin D.C.
      Cell. Mol. Life Sci. 66:1850-1857(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN WNT SIGNALING.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13; SER-18; SER-21 AND SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor."
      Nakaniwa T., Kinoshita T., Sekiguchi Y., Tada T., Nakanishi I., Kitaura K., Suzuki Y., Ohno H., Hirasawa A., Tsujimoto G.
      Acta Crystallogr. F 65:75-79(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-334 IN COMPLEX WITH INHIBITOR.
    18. "Structure of the human protein kinase CK2 catalytic subunit CK2alpha' and interaction thermodynamics with the regulatory subunit CK2beta."
      Bischoff N., Olsen B., Raaf J., Bretner M., Issinger O.G., Niefind K.
      J. Mol. Biol. 407:1-12(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
    19. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-188.

    Entry informationi

    Entry nameiCSK22_HUMAN
    AccessioniPrimary (citable) accession number: P19784
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Can use both ATP and GTP as phosphoryl donors. Phosphorylation by casein kinase 2 has been estimated to represent up to one quarter of the eukaryotic phosphoproteome.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3